ID CARB_STRP4 Reviewed; 1058 AA.
AC B5E512;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
DE RecName: Full=Carbamoyl-phosphate synthase large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; OrderedLocusNames=SPG_1169;
OS Streptococcus pneumoniae serotype 19F (strain G54).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=512566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RX PubMed=11442348; DOI=10.1089/10766290152044995;
RA Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT "Annotated draft genomic sequence from a Streptococcus pneumoniae type
RT 19F clinical isolate.";
RL Microb. Drug Resist. 7:99-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G54;
RA Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G.,
RA Davidsen T.M., Tettelin H., Oggioni M.;
RT "Pneumococcal beta glucoside metabolism investigated by whole genome
RT comparison.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC carbamoyl phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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DR EMBL; CP001015; ACF56322.1; -; Genomic_DNA.
DR RefSeq; YP_002037878.1; NC_011072.1.
DR STRING; 512566.SPG_1169; -.
DR EnsemblBacteria; ACF56322; ACF56322; SPG_1169.
DR GeneID; 6479397; -.
DR KEGG; spx:SPG_1169; -.
DR PATRIC; 19687961; VBIStrPne77426_1231.
DR eggNOG; COG0458; -.
DR HOGENOM; HOG000234582; -.
DR KO; K01955; -.
DR OMA; PMANLAT; -.
DR ProtClustDB; PRK05294; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 2.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR016185; PreATP-grasp_dom.
DR Pfam; PF00289; CPSase_L_chain; 2.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT CHAIN 1 1058 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_1000138899.
FT DOMAIN 133 327 ATP-grasp 1.
FT DOMAIN 671 861 ATP-grasp 2.
FT NP_BIND 159 216 ATP (By similarity).
FT NP_BIND 697 754 ATP (By similarity).
FT REGION 1 401 Carboxyphosphate synthetic domain.
FT REGION 402 546 Oligomerization domain.
FT REGION 547 929 Carbamoyl phosphate synthetic domain.
FT REGION 930 1058 Allosteric domain.
FT METAL 284 284 Magnesium or manganese 1 (By similarity).
FT METAL 298 298 Magnesium or manganese 1 (By similarity).
FT METAL 298 298 Magnesium or manganese 2 (By similarity).
FT METAL 300 300 Magnesium or manganese 2 (By similarity).
FT METAL 820 820 Magnesium or manganese 3 (By similarity).
FT METAL 832 832 Magnesium or manganese 3 (By similarity).
FT METAL 832 832 Magnesium or manganese 4 (By similarity).
FT METAL 834 834 Magnesium or manganese 4 (By similarity).
SQ SEQUENCE 1058 AA; 116242 MW; 883374204E084339 CRC64;
MPKRTDIQKI MVIGSGPIII GQAAEFDYAG TQACLSLKEE GYEVVLVNSN PATIMTDKEI
ADKVYIEPIT LEFVTRILRK ERPDALLPTL GGQTGLNMAM ELSKNGILDE LGVELLGTRL
SAIDQAEDRD LFKQLMEELE QPIPESEIVN TVEEAIAFAA TIGYPVIVRP AFTLGGTGGG
MCANEKELRE ITENGLKLSP VTQCLIERSI AGFKEIEYEV MRDSADNALV VCNMENFDPV
GIHTGDSIVF APAQTMSDYE NQMLRDASLS IIRALKIEGG CNVQLALDPN SFKYYVIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVINPVTG STYAMFEPAL DYVVAKIPRF
PFDKFEKGER RLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVHHNEIP ELAAVSDDTL
IEKVVKAQDD RLFYVSEAIR RGYTPEEIAE LTKIDIFYLD KLLHIFEIEQ ELGAHPQDLE
VLKIAKLNGF SDRKIAELWG TTDDQVRQLR LENKIVPVYK MVDTCAAEFD SETPYFYSTY
GWENESIRSD KESVLVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
DFSVSDKLYF EPLTFEDVMN VIDLEQPKGV IVQFGGQTAI NLAEPLAKAG VTILGTQVAD
LDRAEDRDLF EQALKELDIP QPPGQTATNE EEAALAARKI GFPVLVRPSY VLGGRAMEIV
ENEEDLRSYM RTAVKASPDH PVLVDSYIVG QECEVDAISD GKNVLIPGIM EHIERAGVHS
GDSMAVYPPQ TLSQKVQETI ADYTKRLAIG LHCLGMMNIQ FVIKDEKVYV IEVNPRASRT
VPFLSKVTNI PMAQVATKLI LGQSLSELGY QNGLYPESTR VHIKAPVFSF TKLAKVDSLL
GPEMKSTGEV MGSDATLEKA LYKAFEASYL HLPTFGNVVF TIADDAKEEA LNLARRFQNI
GYGILATEGT AAFFASHGLQ AQPVGKIGDD DKDIPSFVRK GRIQAIINTV GTKRTADEDG
EQIRRSAIEH GVPLFTALDT ANAMLKVLES RSFVTEAI
//
